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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Amino Sugars Reshape Interactions between Streptococcus mutans and Streptococcus gordonii.

Lulu Chen1,2, Alejandro R Walker1, Robert A Burne1

  • 1Department of Oral Biology, University of Florida, College of Dentistry, Gainesville, Florida, USA.

Applied and Environmental Microbiology
|October 24, 2020
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Summary

Amino sugars like glucosamine (GlcN) significantly alter oral bacteria gene expression and metabolism, impacting interactions between beneficial and pathogenic species. GlcN reshapes bacterial communities more than N-acetylglucosamine (GlcNAc), influencing dental caries development.

Keywords:
amino sugarcommensal bacteriadental cariespyruvate metabolismtranscriptomic analysis

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Area of Science:

  • Microbiology and Oral Health
  • Bacterial Metabolism and Ecology

Background:

  • Amino sugars, glucosamine (GlcN) and N-acetylglucosamine (GlcNAc), are key nutrients in the oral cavity.
  • These sugars may confer ecological advantages to commensal bacteria over pathogens.
  • Understanding their impact on oral streptococci is crucial for dental caries research.

Purpose of the Study:

  • To investigate the transcriptomic effects of GlcN and GlcNAc on *Streptococcus mutans* and *Streptococcus gordonii*.
  • To analyze how these amino sugars influence interspecies interactions in dual-species cultures.
  • To determine the role of carbohydrate metabolism in oral biofilm dynamics and pathogenicity.

Main Methods:

  • Transcriptome analysis (RNA deep-sequencing) of *S. mutans* and *S. gordonii*.
  • Single-species and dual-species cultures using glucose, GlcN, or GlcNAc as the primary carbohydrate source.
  • Measurement of pyruvate in culture supernatants.

Main Results:

  • GlcN induced significant transcriptomic shifts in both species, distinct from glucose or GlcNAc.
  • GlcN dramatically altered gene expression in cocultures compared to single-species cultures.
  • GlcN affected pyruvate metabolism genes and inhibited mutacin production in *S. mutans*; GlcN and cocultivation with *S. gordonii* increased manganese transporter genes in *S. mutans*.

Conclusions:

  • Amino sugars, particularly GlcN, profoundly reprogram central metabolism in oral streptococci.
  • These metabolic alterations significantly modify interspecies interactions within oral biofilms.
  • Findings offer insights into carbohydrate metabolism's role in oral health and disease, valuable for developing prevention strategies.